Gotowe bibliografie tematyczne / Viroplasm Structures (VSs)

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  1. Artykuły w czasopismach
  2. Rozprawy doktorskie

Gotowa bibliografia na temat „Viroplasm Structures (VSs)”

Autor: Grafiati
Data publikacji: 6 września 2023

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Artykuły w czasopismach na temat "Viroplasm Structures (VSs)"

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Arnoldi, F., M. Campagna, C. Eichwald, U. Desselberger, and O. R. Burrone. "Interaction of Rotavirus Polymerase VP1 with Nonstructural Protein NSP5 Is Stronger than That with NSP2." Journal of Virology 81, no. 5 (2006): 2128–37. http://dx.doi.org/10.1128/jvi.01494-06.

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ABSTRACT Rotavirus morphogenesis starts in intracellular inclusion bodies called viroplasms. RNA replication and packaging are mediated by several viral proteins, of which VP1, the RNA-dependent RNA polymerase, and VP2, the core scaffolding protein, were shown to be sufficient to provide replicase activity in vitro. In vivo, however, viral replication complexes also contain the nonstructural proteins NSP2 and NSP5, which were shown to be essential for replication, to interact with each other, and to form viroplasm-like structures (VLS) when coexpressed in uninfected cells. In order to gain a b
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Sen, Adrish, Nandini Sen, and Erich R. Mackow. "The Formation of Viroplasm-Like Structures by the Rotavirus NSP5 Protein Is Calcium Regulated and Directed by a C-Terminal Helical Domain." Journal of Virology 81, no. 21 (2007): 11758–67. http://dx.doi.org/10.1128/jvi.01124-07.

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ABSTRACT The rotavirus NSP5 protein directs the formation of viroplasm-like structures (VLS) and is required for viroplasm formation within infected cells. In this report, we have defined signals within the C-terminal 21 amino acids of NSP5 that are required for VLS formation and that direct the insolubility and hyperphosphorylation of NSP5. Deleting C-terminal residues of NSP5 dramatically increased the solubility of N-terminally tagged NSP5 and prevented NSP5 hyperphosphorylation. Computer modeling and analysis of the NSP5 C terminus revealed the presence of an amphipathic α-helix spanning 2
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Mohan, K. V. K., J. Muller, and C. D. Atreya. "The N- and C-Terminal Regions of Rotavirus NSP5 Are the Critical Determinants for the Formation of Viroplasm-Like Structures Independent of NSP2." Journal of Virology 77, no. 22 (2003): 12184–92. http://dx.doi.org/10.1128/jvi.77.22.12184-12192.2003.

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ABSTRACT Molecular events and the interdependence of the two rotavirus nonstructural proteins, NSP5 and NSP2, in producing viroplasm-like structures (VLS) were previously evaluated by using transient cellular coexpression of the genes for the two proteins, and VLS domains as well as the NSP2-binding region of NSP5 were mapped in the context of NSP2. Review of the previous studies led us to postulate that NSP2 binding of NSP5 may block the N terminus of NSP5 or render it inaccessible and that any similar N-terminal blockage may render NSP5 alone capable of producing VLS independent of NSP2. Thi
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Lopez, Nora, Gabriela Camporeale, Mariano Salgueiro, et al. "Deconstructing virus condensation." PLOS Pathogens 17, no. 10 (2021): e1009926. http://dx.doi.org/10.1371/journal.ppat.1009926.

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Viruses have evolved precise mechanisms for using the cellular physiological pathways for their perpetuation. These virus-driven biochemical events must be separated in space and time from those of the host cell. In recent years, granular structures, known for over a century for rabies virus, were shown to host viral gene function and were named using terms such as viroplasms, replication sites, inclusion bodies, or viral factories (VFs). More recently, these VFs were shown to be liquid-like, sharing properties with membrane-less organelles driven by liquid–liquid phase separation (LLPS) in a
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Lopez, Nora, Gabriela Camporeale, Mariano Salgueiro, et al. "Deconstructing virus condensation." PLOS Pathogens 17, no. 10 (2021): e1009926. http://dx.doi.org/10.1371/journal.ppat.1009926.

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Viruses have evolved precise mechanisms for using the cellular physiological pathways for their perpetuation. These virus-driven biochemical events must be separated in space and time from those of the host cell. In recent years, granular structures, known for over a century for rabies virus, were shown to host viral gene function and were named using terms such as viroplasms, replication sites, inclusion bodies, or viral factories (VFs). More recently, these VFs were shown to be liquid-like, sharing properties with membrane-less organelles driven by liquid–liquid phase separation (LLPS) in a
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Buttafuoco, Antonino, Kevin Michaelsen, Kurt Tobler, Mathias Ackermann, Cornel Fraefel, and Catherine Eichwald. "Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm." Journal of Virology 94, no. 7 (2020). http://dx.doi.org/10.1128/jvi.01965-19.

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ABSTRACT One step of the life cycle common to all rotaviruses (RV) studied so far is the formation of viroplasms, membrane-less cytosolic inclusions providing a microenvironment for early morphogenesis and RNA replication. Viroplasm-like structures (VLS) are simplified viroplasm models consisting of complexes of nonstructural protein 5 (NSP5) with the RV core shell VP2 or NSP2. We identified and characterized the domains required for NSP5-VP2 interaction and VLS formation. VP2 mutations L124A, V865A, and I878A impaired both NSP5 hyperphosphorylation and NSP5/VP2 VLS formation. Moreover, NSP5-V
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Dhillon, Poonam, and C. Durga Rao. "Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and Their Sequestration in Viroplasms To Promote Progeny Virus Production." Journal of Virology 92, no. 24 (2018). http://dx.doi.org/10.1128/jvi.01363-18.

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ABSTRACTRotavirus replicates in unique virus-induced cytoplasmic inclusion bodies called viroplasms (VMs), the composition and structure of which have yet to be understood. Based on the analysis of a few proteins, earlier studies reported that rotavirus infection inhibits stress granule (SG) formation and disrupts P bodies (PBs). However, the recent demonstration that rotavirus infection induces cytoplasmic relocalization and colocalization with VMs of several nuclear hnRNPs and AU-rich element-binding proteins (ARE-BPs), which are known components of SGs and PBs, suggested the possibility of
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Rozprawy doktorskie na temat "Viroplasm Structures (VSs)"

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Dhillon, Poonam. "Rotavirus Viroplasm Structure (VS) : The First Insights into the Architectural Assembly of the Viral and Host Factors in the VS"." Thesis, 2017. http://etd.iisc.ac.in/handle/2005/4167.

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Rotavirus is a major cause of acute gastroenteritis in infants and young children and responsible for approximately 453,000 infantile deaths per year. Rotaviruses are non-enveloped RNA viruses belonging to the Reoviridae family. The rotavirus genome is composed of 11 segments of double-stranded RNA (dsRNA), enclosed in an icosahedral triple-layered protein capsid, and it encodes six structural proteins (VP) and six non-structural proteins (NSPs). Removal of the outer capsid from the triple-layered particle (TLP) during virus entry into the cell activates the synthesis and extrusion of the vira
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